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Crystal structure of type effector Tse1 C30A mutant from Pseudomonas aeruginousa
Structural highlights
FunctionTSE1_PSEAE Toxin secreted by the H1 type VI (H1-T6SS) secretion system into the periplasm of recipient cells. Degrades peptidoglycan via amidase activity thereby helping itself to compete with other bacteria (PubMed:21776080, PubMed:22700987, PubMed:22813741, PubMed:22931054). To protect itself, the bacterium synthesizes immunity protein Tsi1 that specifically interacts with and inactivates cognate toxin (PubMed:21776080, PubMed:22700987, PubMed:22931054).[1] [2] [3] [4] Publication Abstract from PubMedThe type VI secretion systems (T6SS) have emerging roles in interspecies competition. In order to have an advantage in defense against other organisms, this system in Pseudomonas aeruginosa delivers a peptidoglycan amidase (Tse1) to the periplasmic space of a competitor. An immune protein (Tsi1) is also produced by the bacterium to protect itself from damage caused by Tse1. Tsi1 directly interacts with Tse1. We report that the crystal structure of Tse1 displays a common CHAP protein fold. Strikingly, our structures showed that the third residue in the catalytic triad may be novel as this residue type has not been observed previously. Crystal structure of type VI effector Tse1 from Pseudomonas aeruginosa.,Zhang H, Gao ZQ, Su XD, Dong YH FEBS Lett. 2012 Sep 21;586(19):3193-9. doi: 10.1016/j.febslet.2012.06.036. Epub, 2012 Jun 29. PMID:22750141[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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